Skip to search form
Skip to main content
Skip to account menu
Semantic Scholar
Semantic Scholar's Logo
Search 218,250,716 papers from all fields of science
Search
Sign In
Create Free Account
TIMM9 gene
Known as:
TIM9
, TIM9A
, translocase of inner mitochondrial membrane 9
Expand
National Institutes of Health
Create Alert
Alert
Related topics
Related topics
1 relation
TIMM10 gene
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2016
Highly Cited
2016
The Import of Proteins into the Mitochondrion of Toxoplasma gondii *
Giel G. van Dooren
,
L. M. Yeoh
,
B. Striepen
,
G. McFadden
Journal of Biological Chemistry
2016
Corpus ID: 29093998
Outside of well characterized model eukaryotes, relatively little is known about the translocons that transport proteins across…
Expand
Highly Cited
2008
Highly Cited
2008
Structural and functional requirements for activity of the Tim9-Tim10 complex in mitochondrial protein import.
M. Baker
,
C. Webb
,
+6 authors
M. Ryan
Molecular Biology of the Cell
2008
Corpus ID: 15668421
The Tim9-Tim10 complex plays an essential role in mitochondrial protein import by chaperoning select hydrophobic precursor…
Expand
Highly Cited
2007
Highly Cited
2007
Oxidative folding of small Tims is mediated by site‐specific docking onto Mia40 in the mitochondrial intermembrane space
D. Sideris
,
K. Tokatlidis
Molecular Microbiology
2007
Corpus ID: 22119237
Oxidative folding in the mitochondrial intermembrane space (IMS) is crucial for the import of certain cysteine‐rich IMS proteins…
Expand
Highly Cited
2007
Highly Cited
2007
Conserved motifs reveal details of ancestry and structure in the small TIM chaperones of the mitochondrial intermembrane space.
I. Gentle
,
A. Perry
,
+12 authors
T. Lithgow
Molecular biology and evolution
2007
Corpus ID: 382925
The mitochondrial inner and outer membranes are composed of a variety of integral membrane proteins, assembled into the membranes…
Expand
Highly Cited
2005
Highly Cited
2005
Distinct domains of small Tims involved in subunit interaction and substrate recognition.
M. Vergnolle
,
C. Baud
,
+4 authors
K. Tokatlidis
Journal of Molecular Biology
2005
Corpus ID: 21626755
Highly Cited
2005
Highly Cited
2005
Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically.
Hui Lu
,
Joanna Woodburn
Journal of Molecular Biology
2005
Corpus ID: 29847139
Highly Cited
2004
Highly Cited
2004
Organization and Function of the Small Tim Complexes Acting along the Import Pathway of Metabolite Carriers into Mammalian Mitochondria*
N. Mühlenbein
,
S. Hofmann
,
U. Rothbauer
,
M. Bauer
Journal of Biological Chemistry
2004
Corpus ID: 19566343
Tim9, Tim10a, and Tim10b are members of the family of small Tim proteins located in the intermembrane space of mammalian…
Expand
Highly Cited
2003
Highly Cited
2003
Juxtaposition of the Two Distal CX3C Motifs via Intrachain Disulfide Bonding Is Essential for the Folding of Tim10*
S. Allen
,
Hui Lu
,
David Thornton
,
K. Tokatlidis
Journal of Biological Chemistry
2003
Corpus ID: 42180156
The TIM10 complex, composed of the homologous proteins Tim10 and Tim9, chaperones hydrophobic proteins inserted at the…
Expand
Highly Cited
2002
Highly Cited
2002
Assembly of Tim9 and Tim10 into a Functional Chaperone*
S. Vial
,
Hui Lu
,
+4 authors
K. Tokatlidis
Journal of Biological Chemistry
2002
Corpus ID: 43827964
The TIM10 complex is localized in the mitochondrial intermembrane space and mediates insertion of hydrophobic proteins at the…
Expand
Highly Cited
1999
Highly Cited
1999
Tim9, a new component of the TIM22·54 translocase in mitochondria
A. Adam
,
Maxi Endres
,
C. Sirrenberg
,
F. Lottspeich
,
W. Neupert
,
M. Brunner
EMBO Journal
1999
Corpus ID: 35130541
We have identified Tim9, a new component of the TIM22·54 import machinery, which mediates transport of proteins into the inner…
Expand
By clicking accept or continuing to use the site, you agree to the terms outlined in our
Privacy Policy
(opens in a new tab)
,
Terms of Service
(opens in a new tab)
, and
Dataset License
(opens in a new tab)
ACCEPT & CONTINUE